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-Structure paper
Title | Structure of BipA in GTP form bound to the ratcheted ribosome. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 112, Issue 35, Page 10944-10949, Year 2015 |
Publish date | Sep 1, 2015 |
Authors | Veerendra Kumar / Yun Chen / Rya Ero / Tofayel Ahmed / Jackie Tan / Zhe Li / Andrew See Weng Wong / Shashi Bhushan / Yong-Gui Gao / |
PubMed Abstract | BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly ...BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation. |
External links | Proc Natl Acad Sci U S A / PubMed:26283392 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.31 - 5 Å |
Structure data | EMDB-6396: The structure of BipA in GTP form bound to the ratcheted ribosome EMDB-6397: The structure of BipA in GTP form bound to the ratcheted ribosome PDB-5a9v: PDB-5a9w: PDB-5a9x: PDB-5a9y: |
Chemicals | ChemComp-GCP: ChemComp-GDP: ChemComp-HOH: ChemComp-G4P: ChemComp-NMY: ChemComp-8AN: |
Source |
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Keywords | RIBOSOMAL PROTEIN / RIBOSOME / TRANSLATIONAL GTPASE FACTORS / BIPA / X-RAY CRYSTALLOGRAPHY AND CRYO-ELECTRON MICROSCOPY / PROTEIN |